Association between the intrinsically disordered protein PEX19 and PEX3

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Association between the intrinsically disordered protein PEX19 and PEX3. / Hattula, K.; Hirschberg, D.; Kalkkinen, N.; Butcher, S.J.; Ora, A.

In: PloS one, Vol. 9, No. 7, e103101, 2014, p. 1-10.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Hattula, K, Hirschberg, D, Kalkkinen, N, Butcher, SJ & Ora, A 2014, 'Association between the intrinsically disordered protein PEX19 and PEX3' PloS one, vol. 9, no. 7, e103101, pp. 1-10. https://doi.org/10.1371/journal.pone.0103101

APA

Hattula, K., Hirschberg, D., Kalkkinen, N., Butcher, S. J., & Ora, A. (2014). Association between the intrinsically disordered protein PEX19 and PEX3. PloS one, 9(7), 1-10. [e103101]. https://doi.org/10.1371/journal.pone.0103101

Vancouver

Author

Hattula, K. ; Hirschberg, D. ; Kalkkinen, N. ; Butcher, S.J. ; Ora, A. / Association between the intrinsically disordered protein PEX19 and PEX3. In: PloS one. 2014 ; Vol. 9, No. 7. pp. 1-10.

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@article{453184db0a684024951aa61a9edd93e2,
title = "Association between the intrinsically disordered protein PEX19 and PEX3",
abstract = "In peroxisomes, peroxins (PEXs) 3 and 19 are the principal protein components of the machinery required for early peroxisomal biogenesis. For further insight into the interaction of PEX3 and PEX19, we used hydrogen exchange mass spectrometry to monitor conformational changes during complex formation between PEX3 and PEX19 in vitro. Our data showed that PEX19 remained highly flexible during interaction with PEX3. However, we could detect three changes, one each in the N-and C-terminus along with a small stretch in the middle of PEX19 (F64–L74) which became shielded from hydrogen exchange when interacting with PEX3. PEX3 became more protected from hydrogen exchange in the binding groove for PEX19 with only small changes elsewhere. Most likely the N-terminus of PEX19 initiates the binding to PEX3, and then subtle conformational changes in PEX3 affect the surface of the PEX3 molecule. PEX19 in turn, is stabilized by folding of a short helix and its C-terminal folding core permitting PEX19 to bind to PEX3 with higher affinity than just the N-terminal interaction allows. Thus within the cell, PEX3 is stabilized by PEX19 preventing PEX3 aggregation.",
keywords = "disordered protein, hydrogen exchange, mass spectrometry, peroxin, disordered protein, hydrogen exchange, mass spectrometry, peroxin, disordered protein, hydrogen exchange, mass spectrometry, peroxin",
author = "K. Hattula and D. Hirschberg and N. Kalkkinen and S.J. Butcher and A. Ora",
year = "2014",
doi = "10.1371/journal.pone.0103101",
language = "English",
volume = "9",
pages = "1--10",
journal = "PloS one",
issn = "1932-6203",
number = "7",

}

RIS - Download

TY - JOUR

T1 - Association between the intrinsically disordered protein PEX19 and PEX3

AU - Hattula, K.

AU - Hirschberg, D.

AU - Kalkkinen, N.

AU - Butcher, S.J.

AU - Ora, A.

PY - 2014

Y1 - 2014

N2 - In peroxisomes, peroxins (PEXs) 3 and 19 are the principal protein components of the machinery required for early peroxisomal biogenesis. For further insight into the interaction of PEX3 and PEX19, we used hydrogen exchange mass spectrometry to monitor conformational changes during complex formation between PEX3 and PEX19 in vitro. Our data showed that PEX19 remained highly flexible during interaction with PEX3. However, we could detect three changes, one each in the N-and C-terminus along with a small stretch in the middle of PEX19 (F64–L74) which became shielded from hydrogen exchange when interacting with PEX3. PEX3 became more protected from hydrogen exchange in the binding groove for PEX19 with only small changes elsewhere. Most likely the N-terminus of PEX19 initiates the binding to PEX3, and then subtle conformational changes in PEX3 affect the surface of the PEX3 molecule. PEX19 in turn, is stabilized by folding of a short helix and its C-terminal folding core permitting PEX19 to bind to PEX3 with higher affinity than just the N-terminal interaction allows. Thus within the cell, PEX3 is stabilized by PEX19 preventing PEX3 aggregation.

AB - In peroxisomes, peroxins (PEXs) 3 and 19 are the principal protein components of the machinery required for early peroxisomal biogenesis. For further insight into the interaction of PEX3 and PEX19, we used hydrogen exchange mass spectrometry to monitor conformational changes during complex formation between PEX3 and PEX19 in vitro. Our data showed that PEX19 remained highly flexible during interaction with PEX3. However, we could detect three changes, one each in the N-and C-terminus along with a small stretch in the middle of PEX19 (F64–L74) which became shielded from hydrogen exchange when interacting with PEX3. PEX3 became more protected from hydrogen exchange in the binding groove for PEX19 with only small changes elsewhere. Most likely the N-terminus of PEX19 initiates the binding to PEX3, and then subtle conformational changes in PEX3 affect the surface of the PEX3 molecule. PEX19 in turn, is stabilized by folding of a short helix and its C-terminal folding core permitting PEX19 to bind to PEX3 with higher affinity than just the N-terminal interaction allows. Thus within the cell, PEX3 is stabilized by PEX19 preventing PEX3 aggregation.

KW - disordered protein

KW - hydrogen exchange

KW - mass spectrometry

KW - peroxin

KW - disordered protein

KW - hydrogen exchange

KW - mass spectrometry

KW - peroxin

KW - disordered protein

KW - hydrogen exchange

KW - mass spectrometry

KW - peroxin

UR - http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0103101

U2 - 10.1371/journal.pone.0103101

DO - 10.1371/journal.pone.0103101

M3 - Article

VL - 9

SP - 1

EP - 10

JO - PloS one

JF - PloS one

SN - 1932-6203

IS - 7

M1 - e103101

ER -

ID: 883756